Solution structure and p43 binding of the p38 leucine zipper motif: coiled‐coil interactions mediate the association between p38 and p43

FEBS Letters

Ahn, Hee-Chul¹  Lee, Bong-Jin¹  Kim, Sunghoon¹ 

[1] Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Seoul 151-742, South Korea

关键词: Coiled-coil motif;    Nuclear magnetic resonance;    Macromolecular tRNA synthetase complex;    Protein–protein interaction;    p38LZ;    leucine zipper motif of p38;    CD;    circular dichroism;    NMR;    nuclear magnetic resonance;    ARS;    aminoacyl-tRNA synthetase;    XRS;    ARS of the substrate amino acid X;    TFE;    2;    2;    2-trifluoroethanol;    2D;    two-dimensional;    NOE;    nuclear Overhauser effect;    NOESY;    NOE spectroscopy;    TOCSY;    total correlation spectroscopy;    DQF-COSY;    double quantum filtered correlation spectroscopy;    SDS;    sodium dodecyl sulfate;    PAGE;    polyacrylamide gel electrophoresis;    GCN4LZ;    the leucine zipper dimerization domain from the yeast transcription factor GCN4;    rmsd;    root mean square deviation;   

DOI  :  10.1016/S0014-5793(03)00362-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

p38, which has been suggested to be a scaffold protein for the assembly of a macromolecular tRNA synthetase complex, contains a leucine zipper-like motif. To understand the importance of the leucine zipper-like motif of p38 (p38LZ) in macromolecular assembly, the p38LZ solution structure was investigated by circular dichroism and nuclear magnetic resonance spectroscopy. The solution structure of p38LZ showed an amphipathic α-helical structure and characteristics similar to a coiled-coil motif. The protein–protein interaction mediated by p38LZ was examined by an in vitro binding assay. The p43 protein, another non-synthetase component of the complex, could bind to p38LZ via its N-terminal domain, which is also predicted to have a potential coiled-coil motif. Thus, we propose that the p38–p43 complex would be formed by coiled-coil interactions, and the formation of the binary complex would facilitate the macromolecular assembly of aminoacyl-tRNA synthetases.

【 授权许可】

Unknown